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Investigation on the metal binding sites of a putative Zn(ii) transporter in opportunistic yeast species Candida albicans†
New Journal of Chemistry ( IF 3.3 ) Pub Date : 2018-02-26 00:00:00 , DOI: 10.1039/c8nj00533h
Denise Bellotti 1, 2, 3, 4 , Dorota Łoboda 5, 6, 7, 8 , Magdalena Rowińska-Żyrek 5, 6, 7, 8 , Maurizio Remelli 1, 2, 3, 4
Affiliation  

In the present work, we focus on C4YJH2, a protein sequence of 199 amino acid residues, found in the genome of Candida albicans, and suggested to be involved in metal transport. Candida albicans is a member of the normal human microbiome; under certain circumstances that allow it to grow out of control, it can transform into a very dangerous fungal pathogen. The most probable Zn(II) binding domain of this sequence was identified at its C-terminus, a histidine-rich region, well conserved in numerous fungal Zn(II) transporters. The Zn(II) binding behaviour towards the three peptides Ac-FHEHGHSHSHGSGGGGGG-NH2 (residues 131–148), Ac-SHSHSHSHS-NH2 (residues 157–165), and Ac-FHEHGHSHSHGSGGGGGGSDHSGDSKSHSHSHSHS-NH2 (residues 131–165) was explored by means of different thermodynamic and spectroscopic techniques. Cu(II) was also investigated since this endogenous metal can compete with Zn(II) for the same binding sites. The results indicate that the peptides under investigation have the ability to tightly coordinate Zn(II), at physiological pH, thus suggesting that the whole protein sequence can play a role in Zn(II) acquisition and regulation. Cu(II) is able to form even stronger complexes than Zn(II) but it is normally present in very low concentrations in the biological environment. The competition between Zn(II) and Cu(II) could be exploited to impair the Zn(II) acquisition routes of Candida albicans. Among the two binding sites, the affinity of both Zn(II) and Cu(II) is higher for that located at the residues 131–148, although the coordination geometry is rather different for the two metal ions.

中文翻译:

调查机会性酵母物种白色念珠菌中假定的Zn(ii)转运蛋白的金属结合位点

在目前的工作中,我们专注于C4YJH2,这是一个199个氨基酸残基的蛋白质序列,存在于白色念珠菌的基因组中,并建议与金属运输有关。白色念珠菌是正常人类微生物组的成员。在某些使其无法控制的情况下,它可以转化为非常危险的真菌病原体。该序列最可能的Zn(II)结合结构域是在其C端(富含组氨酸的区域)鉴定的,在许多真菌Zn(II)转运蛋白中都非常保守。三种肽Ac-FHEHGHSHSHGSGGGGGGGG-NH 2(残基131–148),Ac-SHSHSHSHS-NH 2的Zn(II)结合行为(残基157-165)和Ac-FHEHGHSHSHGSGGGGGGGGSDHSGDSKSHSHSHSHSHS-NH 2(残基131-165)通过不同的热力学和光谱技术进行了研究。还研究了Cu(II),因为这种内源性金属可以与Zn(II)竞争相同的结合位点。结果表明,所研究的肽具有在生理pH下紧密协调Zn(II)的能力,因此表明整个蛋白质序列可以在Zn(II)的获取和调节中发挥作用。Cu(II)能够形成比Zn(II)更强的配合物),但在生物环境中通常以非常低的浓度存在。Zn(II)和Cu(II)之间的竞争可被利用来削弱白色念珠菌的Zn(II)获取途径在两个结合位点中,Zn(II)和Cu(II)的亲和力对位于残基131-148处的亲和力都较高,尽管这两种金属离子的配位几何形状差异很大。
更新日期:2018-02-26
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